Literature DB >> 7689808

Structural studies of complexed FK-506 binding protein.

J Clardy1.   

Abstract

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Year:  1993        PMID： 7689808     DOI： 10.1111/j.1749-6632.1993.tb35848.x

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN： 0077-8923            Impact factor:   5.691


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  4 in total

1.  Structure and activity of the peptidyl-prolyl isomerase domain from the histone chaperone Fpr4 toward histone H3 proline isomerization.

Authors:  Yoan R Monneau; Heddy Soufari; Christopher J Nelson; Cameron D Mackereth
Journal:  J Biol Chem       Date:  2013-07-25       Impact factor: 5.157

2.  Escherichia coli and other species of the Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins.

Authors:  S M Horne; K D Young
Journal:  Arch Microbiol       Date:  1995-05       Impact factor: 2.552

3.  Structure comparison of native and mutant human recombinant FKBP12 complexes with the immunosuppressant drug FK506 (tacrolimus).

Authors:  S Itoh; M A Navia
Journal:  Protein Sci       Date:  1995-11       Impact factor: 6.725

Review 4.  The chemistry of signal transduction.

Authors:  J Clardy
Journal:  Proc Natl Acad Sci U S A       Date:  1995-01-03       Impact factor: 11.205
  4 in total

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